ID G0PHD7_CAEBE Unreviewed; 639 AA.
AC G0PHD7;
DT 19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT 19-OCT-2011, sequence version 1.
DT 27-MAR-2024, entry version 46.
DE RecName: Full=2-hydroxyacyl-CoA lyase 2 {ECO:0000256|ARBA:ARBA00018936};
DE AltName: Full=IlvB-like protein {ECO:0000256|ARBA:ARBA00030510};
GN ORFNames=CAEBREN_24974 {ECO:0000313|EMBL:EGT56227.1};
OS Caenorhabditis brenneri (Nematode worm).
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=135651 {ECO:0000313|Proteomes:UP000008068};
RN [1] {ECO:0000313|Proteomes:UP000008068}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PB2801 {ECO:0000313|Proteomes:UP000008068};
RG Caenorhabditis brenneri Sequencing and Analysis Consortium;
RA Wilson R.K.;
RL Submitted (JUL-2011) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(2R)-hydroxyhexadecanoyl-CoA = formyl-CoA + pentadecanal;
CC Xref=Rhea:RHEA:55212, ChEBI:CHEBI:17302, ChEBI:CHEBI:57376,
CC ChEBI:CHEBI:138654; Evidence={ECO:0000256|ARBA:ARBA00000244};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:55213;
CC Evidence={ECO:0000256|ARBA:ARBA00000244};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2-hydroxyoctadecanoyl-CoA = formyl-CoA + heptadecanal;
CC Xref=Rhea:RHEA:55196, ChEBI:CHEBI:57376, ChEBI:CHEBI:74116,
CC ChEBI:CHEBI:138631; Evidence={ECO:0000256|ARBA:ARBA00000194};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:55197;
CC Evidence={ECO:0000256|ARBA:ARBA00000194};
CC -!- COFACTOR:
CC Name=thiamine diphosphate; Xref=ChEBI:CHEBI:58937;
CC Evidence={ECO:0000256|ARBA:ARBA00001964};
CC -!- SIMILARITY: Belongs to the TPP enzyme family.
CC {ECO:0000256|ARBA:ARBA00007812, ECO:0000256|RuleBase:RU362132}.
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DR EMBL; GL380474; EGT56227.1; -; Genomic_DNA.
DR AlphaFoldDB; G0PHD7; -.
DR STRING; 135651.G0PHD7; -.
DR EnsemblMetazoa; CBN24974.1; CBN24974.1; WBGene00163699.
DR eggNOG; KOG1185; Eukaryota.
DR HOGENOM; CLU_013748_3_3_1; -.
DR InParanoid; G0PHD7; -.
DR OMA; AQMLHVY; -.
DR Proteomes; UP000008068; Unassembled WGS sequence.
DR GO; GO:0003824; F:catalytic activity; IEA:InterPro.
DR GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR GO; GO:0030976; F:thiamine pyrophosphate binding; IEA:InterPro.
DR CDD; cd02004; TPP_BZL_OCoD_HPCL; 1.
DR CDD; cd07035; TPP_PYR_POX_like; 1.
DR Gene3D; 3.40.50.970; -; 2.
DR Gene3D; 3.40.50.1220; TPP-binding domain; 1.
DR InterPro; IPR029035; DHS-like_NAD/FAD-binding_dom.
DR InterPro; IPR029061; THDP-binding.
DR InterPro; IPR012000; Thiamin_PyroP_enz_cen_dom.
DR InterPro; IPR012001; Thiamin_PyroP_enz_TPP-bd_dom.
DR InterPro; IPR000399; TPP-bd_CS.
DR InterPro; IPR045229; TPP_enz.
DR InterPro; IPR011766; TPP_enzyme_TPP-bd.
DR PANTHER; PTHR18968:SF166; 2-HYDROXYACYL-COA LYASE 2; 1.
DR PANTHER; PTHR18968; THIAMINE PYROPHOSPHATE ENZYMES; 1.
DR Pfam; PF02775; TPP_enzyme_C; 1.
DR Pfam; PF00205; TPP_enzyme_M; 1.
DR Pfam; PF02776; TPP_enzyme_N; 1.
DR SUPFAM; SSF52467; DHS-like NAD/FAD-binding domain; 1.
DR SUPFAM; SSF52518; Thiamin diphosphate-binding fold (THDP-binding); 2.
DR PROSITE; PS00187; TPP_ENZYMES; 1.
PE 3: Inferred from homology;
KW Reference proteome {ECO:0000313|Proteomes:UP000008068};
KW Thiamine pyrophosphate {ECO:0000256|RuleBase:RU362132}.
FT DOMAIN 57..170
FT /note="Thiamine pyrophosphate enzyme N-terminal TPP-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02776"
FT DOMAIN 277..408
FT /note="Thiamine pyrophosphate enzyme central"
FT /evidence="ECO:0000259|Pfam:PF00205"
FT DOMAIN 473..624
FT /note="Thiamine pyrophosphate enzyme TPP-binding"
FT /evidence="ECO:0000259|Pfam:PF02775"
SQ SEQUENCE 639 AA; 69363 MW; C7C67C7A2B4327E9 CRC64;
MVLFLVIIVI IIGLLLWKWL DIRSTDELTN MLKLVSSGNG QHVLSNAFQV DEKSKRHGGE
LVASVLKAHD VEEIFVLCGG HISPILVAAE KLGIKIVDTR HEVTAVFAAD AVARLRQSIG
VAAVTAGPGL TNTITAVKNA QMAESPLLLI GGAAPTLLKG RGALQDIDQM VLFRPLCKYV
ARVERLRDIV PTVREAIKAA KSGCPGPVFV EFPVDVLYPY ELVVKEIGFN PNAKGFIQKA
LNFYLRCHVS RQFSSAWLPQ PITPLPTSIP MPKSEQIQEI VQLVKSAKRP VLLIGSQATL
PPVKPADLVK AVEALGCPVF LGGMARGLLG KDHPLQMRQV RRDALKDADL TILAGTVCDF
RLSYGRTLSK KSKIVALNRN YSQLTKNEKA FWNSNVSIQA DVATSLVQVA NALGSNHSKP
TEWVKTLREK DDEKEAANAK KIEQKMSNGF LNPLNFLKTL DQSLPDDAIL VADGGDFVGS
AAYIVRPRGP LQWLDPGAFG TLGVGGGFAL GAKTVYPKRP VYIIWGDGSC GYSLMEYDTF
ARHKLPVIGI VGNDACWTQI AREQVPMFQS SVAVDLARTR YDNVAKSLGS WGETIDETNA
ESARKVLDEA LAVCRSGQQS ALVNVLIGKT DFREGSISV
//
